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• W2087687965 endingPage "8860" @default.
• W2087687965 startingPage "8851" @default.
• W2087687965 abstract "Similarity among food allergens is a great problem affecting the specificity of diagnosis and treatment of allergic patients. We have observed that 80% of patients with food (including wheat) and pollen allergies have increased IgE antibodies against rice proteins. By immunoblotting, we documented that boiling decreased solubility and IgE reactivity of PBS-extracted rice and wheat proteins, yet in SDS extracts this reactivity was only slightly changed. The sera of patients highly positive on the IgE immunoblot and positive in basophil activation and skin prick test with boiled rice components were used for characterizing the IgE-binding proteins separated by 1D or 2D electrophoresis. Using mass spectrometry, we identified 22 rice SDS soluble proteins. Six of them were new thermostable potential rice allergens: glutelin C precursor, granule-bound starch synthase 1 protein, disulfide isomerase-like 1-1 protein, hypothetical protein OsI_13867, putative acid phosphatase precursor 1, and a protein encoded by locus Os02g0453600. All of the identified rice proteins differed from known wheat allergens, except proteins belonging to the α-amylase/trypsin inhibitor family. Furthermore, we would suggest that in patients with high IgE reactivity to wheat and rice components, the IgE immunoblot and skin prick test with boiled rice proteins could be beneficial before diet recommendation." @default.
• W2087687965 created "2016-06-24" @default.
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• W2087687965 date "2013-09-09" @default.
• W2087687965 modified "2023-10-03" @default.
• W2087687965 title "Identification of Rice Proteins Recognized by the IgE Antibodies of Patients with Food Allergies" @default.
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• W2087687965 doi "https://doi.org/10.1021/jf402759f" @default.
• W2087687965 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24016103" @default.
• W2087687965 hasPublicationYear "2013" @default.
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